ID   LYTS_ENTFA              Reviewed;         589 AA.
AC   Q82Z75;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Sensor protein LytS;
DE            EC=2.7.13.3;
GN   Name=lytS; OrderedLocusNames=EF_3197;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Member of the two-component regulatory system LytS/LytT that
CC       probably regulates genes involved in cell wall metabolism.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AE016830; AAO82869.1; -; Genomic_DNA.
DR   RefSeq; NP_816799.1; NC_004668.1.
DR   RefSeq; WP_002354827.1; NC_004668.1.
DR   AlphaFoldDB; Q82Z75; -.
DR   SMR; Q82Z75; -.
DR   STRING; 226185.EF_3197; -.
DR   EnsemblBacteria; AAO82869; AAO82869; EF_3197.
DR   KEGG; efa:EF3197; -.
DR   PATRIC; fig|226185.45.peg.383; -.
DR   eggNOG; COG3275; Bacteria.
DR   HOGENOM; CLU_020473_3_3_9; -.
DR   OMA; SHFFRSN; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF13492; GAF_3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..589
FT                   /note="Sensor protein LytS"
FT                   /id="PRO_0000074790"
FT   TRANSMEM        4..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          238..363
FT                   /note="GAF"
FT   DOMAIN          363..580
FT                   /note="Histidine kinase"
FT   MOD_RES         390
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   589 AA;  64909 MW;  C2A4C9C12CDBA918 CRC64;
     MVELFILMME RVGLIILLAF LLVNVPYFKR VLLSREKMSS KVQLILIFGL FAIISNFTGI
     EIAKNQIVPN NLLTYLSSNA SIANTRTLVI GVSGLVGGPI VGSAVGLIAG FHRVIQGGGH
     SFFYVPASLI VGLIAGFLGS RMAKQTVFPS AGFSAIVGAC MEMIQMIFIF FFSGDLSDGA
     TLVRFIALPM ILLNSVGTFI FMSILTTTLK QEEQAKAVQT HDVLELAAET LPYFREGLNK
     NSSKKVAEII KHYTKVSAIS MTNSHQILAH VGAGSDHHIP ELEVITELSR EVLRTGRMTI
     AHAKEEVGCS DPNCPLQAAI VIPLFSHQQI VGTLKMYFTD PAQLTHVEEQ LAEGLGTIFS
     SQIELGEAEV QSKLLKEAEI KSLQAQVNPH FFFNAINTIS ALMRKDSEKA RKLLLQLSKY
     FRGNLQGAVQ TTIPVSQELE QVKAYLSLEQ ARFPNRYQVT FDVEEAVASE KVPPYAIQVL
     VENTIKHAFG SRKENNQVRV VVKAKQHKLH VDVYDNGQGI PEERRLLLGK TTVTSEKGTG
     TALENLSRRM ANLYGSEGCF LIENLETGGS HVHLEIPMEQ EELDARINR